2e3x

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Russell's viper venom metalloproteinase

Structural highlights

2e3x is a 3 chain structure with sequence from Daboia siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.91Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VM3CX_DABSI Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Russell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 A resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases.

Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases.,Takeda S, Igarashi T, Mori H FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen HS, Chen JM, Lin CW, Khoo KH, Tsai IH. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 2008 Aug;275(15):3944-58. Epub 2008 Jul 4. PMID:18616470 doi:http://dx.doi.org/EJB6540
↑ Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 2007 Dec 22;581(30):5859-64. Epub 2007 Dec 3. PMID:18060879 doi:10.1016/j.febslet.2007.11.062

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2e3x"

Categories: Daboia siamensis | Large Structures | Igarashi T | Takeda S

@@ Line 3: / Line 3: @@
 <StructureSection load='2e3x' size='340' side='right'caption='[[2e3x]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E3X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2e3x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E3X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.91&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Russellysin Russellysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.58 3.4.24.58] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GM6:3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE'>GM6</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e3x OCA], [https://pdbe.org/2e3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e3x RCSB], [https://www.ebi.ac.uk/pdbsum/2e3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e3x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/VM3CX_DABSI VM3CX_DABSI]] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.<ref>PMID:18616470</ref>  [[https://www.uniprot.org/uniprot/SLLC1_DABSI SLLC1_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref>  [[https://www.uniprot.org/uniprot/SLLC2_DABSI SLLC2_DABSI]] Regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The enzyme activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. May serve as an exosite by which the enzyme recognizes and binds to the Gla domain of factor X (F10) and factor IX (F9) in a calcium-dependent manner.<ref>PMID:18616470</ref>
+[https://www.uniprot.org/uniprot/VM3CX_DABSI VM3CX_DABSI] Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.<ref>PMID:18616470</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/2e3x_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Daboia russellii siamensis]]
+[[Category: Daboia siamensis]]
 [[Category: Large Structures]]
-[[Category: Russellysin]]
+[[Category: Igarashi T]]
-[[Category: Igarashi, T]]
+[[Category: Takeda S]]
-[[Category: Takeda, S]]
-[[Category: Blood clotting]]
-[[Category: C-type lectin]]
-[[Category: Disintegrin]]
-[[Category: Hydrolase]]
-[[Category: Metalloproteinase]]
-[[Category: Toxin]]

2e3x

From Proteopedia

Current revision

Crystal structure of Russell's viper venom metalloproteinase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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